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Clinical Chemistry 18: 97-104, 1972;
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Clinical Chemistry, Vol 18, 97-104, Copyright © 1972 by the American Association for Clinical Chemistry

Study of Optimum Buffer Conditions for Measuring Alkaline Phosphatase Activity in Human Serum

Robert B. McComb 1 and George N. Bowers Jr. 1

1 Clinical Chemistry Laboratory, Department of Pathology, Hartford Hospital, Hartford, Conn. 06115.

We have compared 23 compounds, with and without transphosphorylating properties, as buffer systems for human serum alkaline phosphatase activity, with p-nitrophenylphosphate as substrate. Relative enzyme activity in four representative buffers at near-optimal conditions was ethylaminoethanol > diethanolamine > 2-amino-2-methyl-1-propanol > carbonate. Transphosphorylation was demonstrated in the two buffers in which the enzyme was most active, ethylaminoethanol and diethanolamine. The optima for pH, buffer concentration, and substrate for these four systems were studied in detail. 2-Ethylaminoethanol supports the highest enzyme activity of any of the compounds tested. Diethanolamine was shown to have many of the favorable characteristics required for a reference enzyme procedure.


Key Words: amino alcohol and amine buffers • transphosphorylation • p-nitrophenylphosphate substrate • factors affecting enzyme activity • inhibiting effect of primary amine group

Submitted on August 16, 1971
Accepted on October 1, 1971




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